The Herpes Simplex Virus protein ICP47 is a cytosolic protein that specifically inhibits the TAP peptide transporter. This inhibition prevents the presentation of antigenic peptide on the cell surface, thus enabling the virus to evade detection by immune surveillance. Our goal has been to obtain structural information on ICP47, but others and we have found that the protein is actually unfolded/structureless in solution. Only in the presence of membrane or detergent does ICP47 assume any secondary structure. We have performed 3D '5N-edited NOESY and TOCSY experiments with "N-labeled protein produced in E. coli and have found that there are a large number of chemical shift changes in the detergent-bound spectrum relative to the unbound spectrum. These spectra show that there are changes in the environments around many of the residues in ICP47 upon binding to a detergent micelle and suggest that if there is any structure to study of ICP47, it is that of the detergent/membrane-bound form.